| Self-assembly of soluble unlinked and cross-linked fibrin oligomers. | |
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MedLine Citation:
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PMID: 22098241 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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Self-assembly of soluble unlinked and cross-linked fibrin oligomers formed from desA-fibrin monomer under the influence of factor XIIIa was studied in the presence of non-denaturing urea concentrations. By methods of elastic and dynamic light scattering combined with analytical ultracentrifugation, desA-fibrin oligomers formed in both the presence and absence of the factor XIIIa were shown to be ensembles consisting of soluble rod-like double-stranded protofibrils with diverse weight and size. Unlinked and cross-linked soluble double-stranded protofibrils can reach the length of 350-450 nm. The structure of soluble covalently-linked protofibrils is stabilized by isopeptide γ-dimers. Electrophoretic data indicate a complete absence of isopeptide bonds between α-chains of desA-fibrin molecules. The molecular mechanism of formation of soluble rod-like fibrin structures and specific features of its covalent stabilization under the influence of factor XIIIa are discussed. |
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Authors:
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M A Rosenfeld; V B Leonova; M I Biryukova; M V Vasileva |
Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Biochemistry. Biokhimii͡a Volume: 76 ISSN: 1608-3040 ISO Abbreviation: Biochemistry Mosc. Publication Date: 2011 Oct |
Date Detail:
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Created Date: 2011-11-21 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0376536 Medline TA: Biochemistry (Mosc) Country: United States |
Other Details:
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Languages: eng Pagination: 1155-63 Citation Subset: IM |
Affiliation:
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Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 119334, Russia. markrosenfeld@rambler.ru. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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